1jdq: Difference between revisions
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==Solution Structure of TM006 Protein from Thermotoga maritima== | ==Solution Structure of TM006 Protein from Thermotoga maritima== | ||
<StructureSection load='1jdq' size='340' side='right' caption='[[1jdq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1jdq' size='340' side='right' caption='[[1jdq]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1jdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1jdq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JDQ FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdq OCA], [http://pdbe.org/1jdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jdq RCSB], [http://www.ebi.ac.uk/pdbsum/1jdq PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdq OCA], [http://pdbe.org/1jdq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jdq RCSB], [http://www.ebi.ac.uk/pdbsum/1jdq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jdq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jdq ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 12:46, 4 October 2017
Solution Structure of TM006 Protein from Thermotoga maritimaSolution Structure of TM006 Protein from Thermotoga maritima
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins. An NMR approach to structural proteomics.,Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30. PMID:11854485[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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